Identification of aaNAT5b as a spermine N-acetyltransferase in the mosquito, Aedes aegypti

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dc.contributor.authorGuan, Huaien
dc.contributor.authorWang, Maoyingen
dc.contributor.authorLiao, Chenghongen
dc.contributor.authorLiang, Jingen
dc.contributor.authorMehere, Prajwalinien
dc.contributor.authorTian, Meilingen
dc.contributor.authorLiu, Hairongen
dc.contributor.authorRobinson, Howarden
dc.contributor.authorLi, Jianyongen
dc.contributor.authorHan, Qianen
dc.contributor.departmentBiochemistryen
dc.date.accessioned2019-06-05T13:02:46Zen
dc.date.available2019-06-05T13:02:46Zen
dc.date.issued2018-03-19en
dc.description.abstractMosquitoes transmit a number of diseases in animals and humans, including Dengue, Chikungunya and Zika viruses that affect millions of people each year. Controlling the disease-transmitting mosquitoes has proven to be a successful strategy to reduce the viruses transmission. Polyamines are required for the life cycle of the RNA viruses, Chikungunya virus and Zika virus, and a depletion of spermidine and spermine in the host via induction of spermine N-acetyltransferase restricts their replication. Spermine N-acetyltransferase is a key catabolic enzyme in the polyamine pathway, however there is no information of the enzyme identification in any insects. Aliphatic polyamines play a fundamental role in tissue growth and development in organisms. They are acetylated by spermidine/spermine N-1-acetyl-transferase (SAT). In this study we provided a molecular and biochemical identification of SAT from Aedes aegypti mosquitoes. Screening of purified recombinant proteins against polyamines established that aaNAT5b, named previously based on sequence similarity with identified aaNAT1 in insects, is active to spermine and spermidine. A crystal structure was determined and used in molecular docking in this study. Key residues were identified to be involved in spermine binding using molecular docking and simulation. In addition, SAT transcript was down regulated by blood feeding using a real time PCR test. Based on its substrate profile and transcriptional levels after blood feeding, together with previous reports for polyamines required in arboviruses replication, SAT might be potentially used as a target to control arboviruses with human interference.en
dc.description.notesThis work was supported by National Natural Science Foundation of China [Grant Number 31472186] (QH). The funders had no role in study design, data collection and analysis, decision to publish, or preparation of the manuscript.en
dc.description.sponsorshipNational Natural Science Foundation of China [31472186]en
dc.format.mimetypeapplication/pdfen
dc.identifier.doihttps://doi.org/10.1371/journal.pone.0194499en
dc.identifier.eissn1932-6203en
dc.identifier.issue3en
dc.identifier.othere0194499en
dc.identifier.pmid29554129en
dc.identifier.urihttp://hdl.handle.net/10919/89756en
dc.identifier.volume13en
dc.language.isoenen
dc.publisherPLOSen
dc.rightsCreative Commons Attribution 4.0 Internationalen
dc.rights.urihttp://creativecommons.org/licenses/by/4.0/en
dc.titleIdentification of aaNAT5b as a spermine N-acetyltransferase in the mosquito, Aedes aegyptien
dc.title.serialPLOS ONEen
dc.typeArticle - Refereeden
dc.type.dcmitypeTexten

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